Curated Information
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Curated Information Page
PubMed Id: 9346908 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
Abdollah S, et al. (1997) TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J Biol Chem 272, 27678-85 9346908
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S464-p - Smad2 (human) ▲
Orthologous residues
Smad2 (human): S464‑p, Smad2 (mouse): S464‑p, Smad2 (rat): S464‑p
Characterization
 Methods used to characterize site in vivo:  2D analysis, mutation of modification site, phospho-antibody, phosphoamino acid analysis, western blotting
 Disease tissue studied:  liver cancer
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HepG2 (hepatic), Mv1Lu (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human

S465-p - Smad2 (human) ▲
Orthologous residues
Smad2 (human): S465‑p, Smad2 (mouse): S465‑p, Smad2 (rat): S465‑p
Characterization
 Methods used to characterize site in vivo:  2D analysis, mutation of modification site, phospho-antibody, phosphoamino acid analysis, western blotting
 Disease tissue studied:  liver cancer
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HepG2 (hepatic), Mv1Lu (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE TGFBR1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE TGFBR1 (human) phosphopeptide analysis, 2D analysis, mutation in upstream enzyme recognition motif, transfection of constitutively active enzyme
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
TGFBR1 (human) Disrupts molecular association, regulation transcription, altered co-immunoprecipitation
Smad4 (human) Induces molecular association, regulation co-immunoprecipitation
 Comments:  S464 not likely phosphorylated but is required for efficient phosphorylation of COOH terminus.

S467-p - Smad2 (human) ▲
Orthologous residues
Smad2 (human): S467‑p, Smad2 (mouse): S467‑p, Smad2 (rat): S467‑p
Characterization
 Methods used to characterize site in vivo:  2D analysis, mutation of modification site, phospho-antibody, phosphoamino acid analysis, western blotting
 Disease tissue studied:  liver cancer
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HepG2 (hepatic), Mv1Lu (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE TGFBR1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE TGFBR1 (human) phosphopeptide analysis, 2D analysis, mutation in upstream enzyme recognition motif, transfection of constitutively active enzyme
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
TGFBR1 (human) Disrupts molecular association, regulation transcription, altered co-immunoprecipitation
Smad4 (human) Induces molecular association, regulation co-immunoprecipitation
 Comments:  S464 not likely phosphorylated but is required for efficient phosphorylation of COOH terminus.


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